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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
37
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pubmed:dateCreated |
2001-9-10
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pubmed:abstractText |
The production of bio-active interleukin-1beta (IL-1beta), a pro-inflammatory cytokine, is mediated by activated caspase-1. One of the known molecular mechanisms underlying pro-caspase-1 processing and activation involves binding of the caspase-1 prodomain to a caspase recruitment domain (CARD)-containing serine/threonine kinase known as RIP2/CARDIAK/RICK. We have identified a novel protein, COP (CARD only protein), which has a high degree of sequence identity to the caspase-1 prodomain. COP binds to both RIP2 and the caspase-1 prodomain and inhibits RIP2-induced caspase-1 oligomerization. COP inhibits caspase- 1-induced IL-1beta secretion as well as lipopolysaccharide-induced IL-1beta secretion in transfected cells. Our data indicate that COP can regulate IL-1beta secretion, implying that COP may play a role in down-regulating inflammatory responses analogous to the CARD protein ICEBERG.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 1,
http://linkedlifedata.com/resource/pubmed/chemical/ICEBERG protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/LLID-114769 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RIPK2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor-Interacting Protein...
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
34495-500
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11432859-Amino Acid Sequence,
pubmed-meshheading:11432859-Base Sequence,
pubmed-meshheading:11432859-Carrier Proteins,
pubmed-meshheading:11432859-Caspase 1,
pubmed-meshheading:11432859-Humans,
pubmed-meshheading:11432859-Interleukin-1,
pubmed-meshheading:11432859-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:11432859-Lipopolysaccharides,
pubmed-meshheading:11432859-Molecular Sequence Data,
pubmed-meshheading:11432859-NF-kappa B,
pubmed-meshheading:11432859-Protein-Serine-Threonine Kinases,
pubmed-meshheading:11432859-RNA, Messenger,
pubmed-meshheading:11432859-Receptor-Interacting Protein Serine-Threonine Kinase 2
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pubmed:year |
2001
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pubmed:articleTitle |
Cop, a caspase recruitment domain-containing protein and inhibitor of caspase-1 activation processing.
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pubmed:affiliation |
Burnham Institute, La Jolla, California 92037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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